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Volume 9, Issue 5 (Suppl)
J Bioequiv Availab, an open access journal
ISSN: 0975-0851
Pharmacy & Biopharma 2017
August 31-September 01, 2017 Philadelphia, USA
August 31-September 01, 2017 Philadelphia, USA
3
rd
International Conference on
Biopharmaceutics and Biologic Drugs
&
5
th
International Pharmacy Conference
J Bioequiv Availab 2017, 9:5 (Suppl)
DOI: 10.4172/0975-0851-C1-031
PhcrTx1, novel marine peptide acting on acid-sensing ion channels and its isolation and characterization
Armando Alexei Rodríguez Alfonso
Hannover Medical School, Germany
A
cid-sensing ion channels (ASICs) are H+-gated Na+ channels that belong to the ENaC/degenerin superfamily of sodium
channels. ASICs are involved in sensory perception, synaptic plasticity, learning, memory formation, cell migration and
proliferation, nociception, and neurodegenerative disorders, among other processes, therefore those molecules that specifically
target these channels are of growing pharmacological and biomedical interest. Sea anemones produce a large variety of ion
channels peptide toxins. However, those acting on ligand-gated ion channels, including acid-sensing ion channel (ASIC)
toxins, remain poorly explored. PhcrTx1 is the first compound characterized from the sea anemone
Phymanthus crucifer
, and
it constitutes a novel ASIC inhibitor. This peptide was purified by liquid chromatographic techniques, followed by biological
evaluation on ion channels of isolated rat dorsal root ganglia (DRG) neurons using patch-clamp techniques. PhcrTx1 partially
inhibited ASIC currents (IC50∼100 nM). The N-terminal sequencing yielded 32 amino acid residues, with a molecular mass of
3477 Da by mass spectrometry. No sequence identity to other sea anemone peptides was found. Interestingly, the bioinformatics
analysis of cys-pattern and secondary structure arrangement suggested that this peptide presents an inhibitor cystine knot
(ICK) scaffold, which has been found in other venomous organisms such as spiders, scorpions, and cone snails. Our results
show that PhcrTx1 represents the first member of a new structural group of sea anemones toxins acting on ASIC. Also, this
peptide constitutes a novel template for the development of drugs against pathologies related to ASICs function.
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